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This section includes 226 Mcqs, each offering curated multiple-choice questions to sharpen your Biochemistry knowledge and support exam preparation. Choose a topic below to get started.
51. |
If the F and Y angles of each peptide unit in a protein are known, which of the following may also be determined? |
A. | Complete secondary structure |
B. | Complete tertiary structure |
C. | Complete quaternary structure |
D. | Thermodynamic stability |
Answer» B. Complete tertiary structure | |
52. |
In β-pleated sheet structures neighbouring |
A. | chains lie in a flat plane |
B. | neighboring residues are hydrogen bonded |
C. | neighboring chains are connected by a-helices |
D. | neighboring chains are hydrogen bonded |
Answer» E. | |
53. |
Individuals with PKU disease are mentally retarded unless |
A. | phenylalanine in the diet is restricted |
B. | tyrosine in the diet is restricted |
C. | homogentisic acid in the diet is restricted |
D. | none of the above |
Answer» B. tyrosine in the diet is restricted | |
54. |
Enzyme required to convert polypeptides to amino acids is |
A. | pepsin |
B. | maltase |
C. | erepsin |
D. | diastase |
Answer» D. diastase | |
55. |
Which of the following statements is true about SDS polyacrylamide chromatography? |
A. | SDS polyacrylamide gel electrophoresis separates proteins on the basis of size |
B. | SDS polyacrylamide gel electrophoresis separates proteins on the basis of charge |
C. | SDS binds to proteins non-covalently with a stoichiometry of around one SDS molecule per three amino acids |
D. | SDS binds to proteins non-covalently with a stoichiometry of around one SDS molecule per one amino acid |
Answer» C. SDS binds to proteins non-covalently with a stoichiometry of around one SDS molecule per three amino acids | |
56. |
Immunoaffinity chromatography can be used in biochemical applications to |
A. | break down antibody structure |
B. | purify protein antigen |
C. | break down antigen and analyze quantitatively |
D. | none of the above |
Answer» C. break down antigen and analyze quantitatively | |
57. |
The peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala, was digested with cyanogen bromide (CNBr) to produce: |
A. | Val-Lys + Glu-Met-Ser + Trp-Arg-Ala |
B. | Val-Lys-Glu-Met-Ser-Trp + Arg-Ala |
C. | Val-Lys-Glu-Met + Ser-Trp-Arg-Ala |
D. | Val-Lys-Glu + Met-Ser-Trp-Arg-Ala |
Answer» D. Val-Lys-Glu + Met-Ser-Trp-Arg-Ala | |
58. |
Since ΔG° = -RTlnK |
A. | a 10-fold increase in K decreases ΔG° by about 10-fold |
B. | a 10-fold decrease in K decreases ΔG° by about 2.3*RT |
C. | a 10-fold increase in K decreases ΔG° by about 2.3*RT |
D. | a 10-fold decrease in K increases ΔG° by about 10-fold |
Answer» D. a 10-fold decrease in K increases ΔG° by about 10-fold | |
59. |
The resonance structures that can be drawn for the peptide bond indicate that the peptide bond |
A. | is stronger than an ordinary single bond |
B. | has partial double bond character |
C. | both (a) and (b) |
D. | is still not completely understood |
Answer» D. is still not completely understood | |
60. |
Which hemoglobin chain replaces the beta chain in embryonic hemoglobulin? |
A. | Delta |
B. | Epsilon |
C. | Gamma |
D. | Alfa |
Answer» C. Gamma | |
61. |
The amino acids used to build proteins in cells can be distinguished through |
A. | C-OH side chain |
B. | C=O bonding |
C. | side chain of R groups |
D. | C-H chain |
Answer» D. C-H chain | |
62. |
For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that |
A. | unfolding is favored enthalpically |
B. | folding is favored enthalpically |
C. | the entropy is positive at all temperatures |
D. | the entropy is negative at all temperatures |
Answer» C. the entropy is positive at all temperatures | |
63. |
In Counter immunoelectrophoresis |
A. | electrophoresis will drive the antibody and antigen parallel to each other |
B. | electrophoresis will drive the antibody and antigen toward each other |
C. | the antibody will migrate towards anode |
D. | the antibody will migrate towards cathode |
Answer» C. the antibody will migrate towards anode | |
64. |
A protein that shows infinite cooperative for binding of n ligands will |
A. | show a Hill coefficient (nH) of 0.0 |
B. | only be found in either the unliganded form or the fully liganded form |
C. | show a Hill coefficient (nH) of n |
D. | both (b) and (c) |
Answer» E. | |
65. |
Secondary structure in protein refers to |
A. | linear sequence of amino acids joined together by peptide bond |
B. | three dimensional arrangement of all amino acids in polypeptide chain |
C. | regular folding of regions of the polypeptide chain |
D. | protein made up of more than one polypeptide chain |
Answer» D. protein made up of more than one polypeptide chain | |
66. |
Reactions of condensation produce polymers e.g. |
A. | peptides |
B. | proteins |
C. | carbonyls |
D. | hydrocarbons |
Answer» C. carbonyls | |
67. |
When a small number of acids or bases are added to zwitterion ion, it resists a change in |
A. | temperature |
B. | volatility |
C. | polarity |
D. | pH |
Answer» E. | |
68. |
The number of amino acids by which human proteins are manufactured is |
A. | twenty |
B. | forty |
C. | twelve |
D. | eight |
Answer» B. forty | |
69. |
The general formula for 2 amino carboxylic acid is |
A. | R-CH(NH₂)COOH |
B. | R-CHCOOH |
C. | R-CH(NH₂) |
D. | R-CH |
Answer» B. R-CHCOOH | |
70. |
The amino acid sequences of thousands of different proteins from many species have been determined using principles first developed by? |
A. | Edman |
B. | Sanger |
C. | Mendel |
D. | Watson and Crick |
Answer» C. Mendel | |
71. |
Metastasis involves |
A. | ability of cells to dissolve cellular matrix |
B. | metalloprotein levels |
C. | decreased levels of proteins that regulate metalloproteins |
D. | all of the above |
Answer» E. | |
72. |
Amino acids are by nature |
A. | acidic |
B. | basic |
C. | amphoteric |
D. | alkalinic |
Answer» D. alkalinic | |
73. |
Proteins are separated in an SDS-PAGE experiment on the basis of their |
A. | positively charged side chains |
B. | molecular weight |
C. | negatively charged side chains |
D. | different isoelectric points |
Answer» C. negatively charged side chains | |
74. |
Peptides in the fully extended chain conformation |
A. | have Y = F = 180° |
B. | do not occur in nature |
C. | also have a cis geometry in their peptide bonds |
D. | are equivalent to the (3-sheet structure |
Answer» B. do not occur in nature | |
75. |
Which of the following statements is true about ion-exchange chromatography? |
A. | It separates proteins according to their size |
B. | The column matrix with bound anionic groups is called cationic exchanger |
C. | The column matrix with bound anionic groups is called anionic exchanger |
D. | The column matrix with bound cationic groups is called cationic exchanger |
Answer» C. The column matrix with bound anionic groups is called anionic exchanger | |
76. |
What is the effect of a decrease in pH on hemoglobin oxygen affinity? |
A. | Decrease in oxygen affinity |
B. | Increase in oxygen affinity |
C. | No effect on oxygen affinity |
D. | Increase affinity in muscle cell otherwise decrease |
Answer» B. Increase in oxygen affinity | |
77. |
If pK1 = 2.34 and pK2 = 9.60, then the isoelectric point pI is? |
A. | 5.87 |
B. | 5.97 |
C. | 3.67 |
D. | 11.94 |
Answer» C. 3.67 | |
78. |
The two amino acids having R groups with a negative net charge at pH 7.0 are ___________ |
A. | Aspartate and glutamate |
B. | Arginine and histidine |
C. | Cysteine and methionine |
D. | Proline and valine |
Answer» B. Arginine and histidine | |
79. |
Polypeptides bear long molecules hence they are represented shorthand by |
A. | three letter abbreviation |
B. | numerals |
C. | Roman numbers |
D. | two letter abbreviations |
Answer» B. numerals | |
80. |
Number of chiral centers in isoleucine is? |
A. | 1 |
B. | 2 |
C. | 3 |
D. | 4 |
Answer» C. 3 | |
81. |
Agarose gel electrophoresis and pulsed field gel electrophoresis may be used to resolve respectively |
A. | 2000 kb and 20kb DNA |
B. | 1000 kb and l0kb DNA |
C. | 20 kb and 2000 kb DNA |
D. | 10 kb and 1000 kb DNA |
Answer» D. 10 kb and 1000 kb DNA | |
82. |
Product formed after reaction between two amino acids is called |
A. | reagent |
B. | peptide |
C. | dipeptide |
D. | poly peptide |
Answer» D. poly peptide | |
83. |
What is the proportion of glycine residues in collagenous regions? |
A. | One-fourth |
B. | One-third |
C. | Half |
D. | One-tenth |
Answer» C. Half | |
84. |
In an SDS-PAGE |
A. | proteins are denatured by the SDS |
B. | proteins have the same charge-to-mass ratio |
C. | smaller proteins migrate more rapidly through the gel |
D. | all of the above |
Answer» E. | |
85. |
Glycine which is a simplest amino acid is |
A. | amino acid |
B. | amino ethanoic acid |
C. | aminate |
D. | amylase |
Answer» C. aminate | |
86. |
Which of the following is an example of tertiary structure in a protein? |
A. | A multimeric protein |
B. | An a-helix |
C. | A P-pleated sheet |
D. | A globular domain |
Answer» E. | |
87. |
Who deduced the double-helical structure of DNA? |
A. | Frederick Sanger |
B. | Mendel |
C. | Watson and Francis Crick |
D. | Anton van Leeuwenhoek |
Answer» D. Anton van Leeuwenhoek | |
88. |
Protein folding is |
A. | automatic, mediated by the protein itself |
B. | mediated by other proteins called chaperones |
C. | mediated by the ribosomes |
D. | none of the above |
Answer» C. mediated by the ribosomes | |
89. |
The four subunits of the hemoglobin (Hb) gene represent protein's |
A. | primary structure |
B. | secondary structure |
C. | tertiary structure |
D. | quaternary structure |
Answer» E. | |
90. |
The nature of peptide bond can be best explained as |
A. | partial double bond |
B. | truly double bond |
C. | Hydrogen bond |
D. | Van der waals force |
Answer» B. truly double bond | |
91. |
Heme is the binding pocket of myoglobin and hemoglobin and is composed of |
A. | negatively charged residues |
B. | polar residues |
C. | hydrophobic residues |
D. | positively charged residues |
Answer» D. positively charged residues | |
92. |
Immunoelectrophoresis techniques are designed to separate the mixture components from each other by using electrophoresis |
A. | prior to reaction with antibody |
B. | prior to reaction with antigen |
C. | after reaction with antibody |
D. | after reaction with antigen |
Answer» B. prior to reaction with antigen | |
93. |
The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues |
A. | reflects the reduction in solvent-accessible area during protein folding |
B. | is only meaningful for the polar amino acids |
C. | ignores the important contribution of the peptide bond |
D. | is similar to effects seen with SDS denaturation |
Answer» B. is only meaningful for the polar amino acids | |
94. |
Which of the following statements is true about two-dimensional electrophoresis? |
A. | Separates proteins of identical molecular weight, same pI but different charge |
B. | Separates proteins of different molecular weight and different pI |
C. | Separates proteins of identical molecular weight that differ in pI |
D. | Isoelectric focusing is also termed as two-dimensional electrophoresis |
Answer» D. Isoelectric focusing is also termed as two-dimensional electrophoresis | |
95. |
Tertiary conformation of proteins is maintained by 3 types of bonds namely ionic, hydrogen and __________ |
A. | Sulfide |
B. | Disulfide |
C. | Covalent |
D. | Peptide |
Answer» C. Covalent | |
96. |
At the midpoint of a temperature transition curve, |
A. | half of the protein is denatured |
B. | Keq = 1.0 and ΔG = 0 |
C. | [Native] = [Unfolded] |
D. | All of these |
Answer» E. | |
97. |
Which among the following is a non-essential amino acid? |
A. | Serine |
B. | Threonine |
C. | Lysine |
D. | Histidine |
Answer» B. Threonine | |
98. |
The competitive immunoassay can be used |
A. | to detect very small amounts of antigen |
B. | to detect antibody associated with allergies (IgE) |
C. | both (a) and (b) |
D. | commonly to detect trace amounts of drugs. |
Answer» D. commonly to detect trace amounts of drugs. | |
99. |
Which of the three subunits of the G proteins binds GDP and GTP? |
A. | Alpha |
B. | Beta |
C. | Gamma |
D. | Delta |
Answer» B. Beta | |
100. |
Zwitterion ions are |
A. | crystalline solid |
B. | soluble in water |
C. | amphoteric |
D. | all of above |
Answer» E. | |